Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P35556 (FBN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrillin-2
Gene names
Name:FBN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2912 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Involvement in disease

Arthrogryposis, distal, 9 (DA9) [MIM:121050]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the fibrillin family.

Contains 47 EGF-like domains.

Contains 9 TB (TGF-beta binding) domains.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.7. Source: ProtInc

bone trabecula formation

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

positive regulation of bone mineralization

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

sequestering of TGFbeta in extracellular matrix

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

microfibril

Traceable author statement PubMed 20855508. Source: BHF-UCL

proteinaceous extracellular matrix

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

extracellular matrix structural constituent

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35556-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35556-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-145: Missing.
     1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
     1507-2912: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 29122884Fibrillin-2
PRO_0000007584

Regions

Domain111 – 14232EGF-like 1
Domain145 – 17632EGF-like 2
Domain176 – 20833EGF-like 3
Domain214 – 26653TB 1
Domain276 – 31742EGF-like 4; calcium-binding
Domain318 – 35942EGF-like 5; calcium-binding
Domain364 – 41754TB 2
Domain494 – 53441EGF-like 6
Domain535 – 57440EGF-like 7; calcium-binding
Domain575 – 61642EGF-like 8; calcium-binding
Domain617 – 65741EGF-like 9; calcium-binding
Domain658 – 69841EGF-like 10; calcium-binding
Domain704 – 75653TB 3
Domain768 – 80942EGF-like 11; calcium-binding
Domain810 – 85142EGF-like 12; calcium-binding
Domain852 – 89140EGF-like 13; calcium-binding
Domain896 – 94752TB 4
Domain955 – 99642EGF-like 14; calcium-binding
Domain1001 – 105252TB 5
Domain1073 – 111442EGF-like 15; calcium-binding
Domain1115 – 115743EGF-like 16; calcium-binding
Domain1158 – 119942EGF-like 17; calcium-binding
Domain1200 – 124142EGF-like 18; calcium-binding
Domain1242 – 128241EGF-like 19; calcium-binding
Domain1283 – 132442EGF-like 20; calcium-binding
Domain1325 – 136642EGF-like 21; calcium-binding
Domain1367 – 140741EGF-like 22; calcium-binding
Domain1408 – 144841EGF-like 23; calcium-binding
Domain1449 – 149042EGF-like 24; calcium-binding
Domain1491 – 153141EGF-like 25; calcium-binding
Domain1532 – 157241EGF-like 26; calcium-binding
Domain1577 – 163357TB 6
Domain1650 – 169142EGF-like 27; calcium-binding
Domain1692 – 173342EGF-like 28; calcium-binding
Domain1738 – 179154TB 7
Domain1808 – 184942EGF-like 29; calcium-binding
Domain1850 – 189142EGF-like 30; calcium-binding
Domain1892 – 193342EGF-like 31; calcium-binding
Domain1934 – 197239EGF-like 32; calcium-binding
Domain1973 – 201543EGF-like 33; calcium-binding
Domain2016 – 205540EGF-like 34; calcium-binding
Domain2056 – 209742EGF-like 35; calcium-binding
Domain2102 – 215554TB 8
Domain2171 – 221242EGF-like 36; calcium-binding
Domain2213 – 225240EGF-like 37; calcium-binding
Domain2253 – 229341EGF-like 38; calcium-binding
Domain2294 – 233744EGF-like 39; calcium-binding
Domain2338 – 237942EGF-like 40; calcium-binding
Domain2384 – 243754TB 9
Domain2449 – 249042EGF-like 41; calcium-binding
Domain2491 – 253141EGF-like 42; calcium-binding
Domain2532 – 257039EGF-like 43; calcium-binding
Domain2571 – 261343EGF-like 44; calcium-binding
Domain2614 – 265340EGF-like 45; calcium-binding
Domain2654 – 269441EGF-like 46; calcium-binding
Domain2695 – 273440EGF-like 47; calcium-binding

Amino acid modifications

Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation11121N-linked (GlcNAc...) Ref.6
Glycosylation14141N-linked (GlcNAc...) Potential
Glycosylation15291N-linked (GlcNAc...) Potential
Glycosylation16251N-linked (GlcNAc...) Potential
Glycosylation17141N-linked (GlcNAc...) Potential
Glycosylation17451N-linked (GlcNAc...) Potential
Glycosylation17561N-linked (GlcNAc...) Potential
Glycosylation19451N-linked (GlcNAc...) Potential
Glycosylation21201N-linked (GlcNAc...) Potential
Glycosylation22251N-linked (GlcNAc...) Potential
Glycosylation28081N-linked (GlcNAc...) Potential
Disulfide bond115 ↔ 124 By similarity
Disulfide bond119 ↔ 130 By similarity
Disulfide bond132 ↔ 141 By similarity
Disulfide bond149 ↔ 159 By similarity
Disulfide bond153 ↔ 164 By similarity
Disulfide bond166 ↔ 175 By similarity
Disulfide bond180 ↔ 190 By similarity
Disulfide bond184 ↔ 196 By similarity
Disulfide bond198 ↔ 207 By similarity
Disulfide bond280 ↔ 292 By similarity
Disulfide bond287 ↔ 301 By similarity
Disulfide bond303 ↔ 316 By similarity
Disulfide bond322 ↔ 334 By similarity
Disulfide bond329 ↔ 343 By similarity
Disulfide bond345 ↔ 358 By similarity
Disulfide bond498 ↔ 510 By similarity
Disulfide bond505 ↔ 519 By similarity
Disulfide bond521 ↔ 533 By similarity
Disulfide bond539 ↔ 549 By similarity
Disulfide bond544 ↔ 558 By similarity
Disulfide bond560 ↔ 573 By similarity
Disulfide bond579 ↔ 591 By similarity
Disulfide bond586 ↔ 600 By similarity
Disulfide bond602 ↔ 615 By similarity
Disulfide bond621 ↔ 632 By similarity
Disulfide bond627 ↔ 641 By similarity
Disulfide bond643 ↔ 656 By similarity
Disulfide bond662 ↔ 673 By similarity
Disulfide bond668 ↔ 682 By similarity
Disulfide bond684 ↔ 697 By similarity
Disulfide bond772 ↔ 784 By similarity
Disulfide bond779 ↔ 793 By similarity
Disulfide bond795 ↔ 808 By similarity
Disulfide bond814 ↔ 826 By similarity
Disulfide bond821 ↔ 835 By similarity
Disulfide bond837 ↔ 850 By similarity
Disulfide bond856 ↔ 866 By similarity
Disulfide bond861 ↔ 875 By similarity
Disulfide bond877 ↔ 890 By similarity
Disulfide bond959 ↔ 971 By similarity
Disulfide bond966 ↔ 980 By similarity
Disulfide bond982 ↔ 995 By similarity
Disulfide bond1077 ↔ 1089 By similarity
Disulfide bond1084 ↔ 1098 By similarity
Disulfide bond1100 ↔ 1113 By similarity
Disulfide bond1119 ↔ 1131 By similarity
Disulfide bond1126 ↔ 1140 By similarity
Disulfide bond1142 ↔ 1156 By similarity
Disulfide bond1162 ↔ 1174 By similarity
Disulfide bond1169 ↔ 1183 By similarity
Disulfide bond1185 ↔ 1198 By similarity
Disulfide bond1204 ↔ 1216 By similarity
Disulfide bond1211 ↔ 1225 By similarity
Disulfide bond1227 ↔ 1240 By similarity
Disulfide bond1246 ↔ 1257 By similarity
Disulfide bond1253 ↔ 1266 By similarity
Disulfide bond1268 ↔ 1281 By similarity
Disulfide bond1287 ↔ 1299 By similarity
Disulfide bond1294 ↔ 1308 By similarity
Disulfide bond1310 ↔ 1323 By similarity
Disulfide bond1329 ↔ 1341 By similarity
Disulfide bond1336 ↔ 1350 By similarity
Disulfide bond1352 ↔ 1365 By similarity
Disulfide bond1371 ↔ 1384 By similarity
Disulfide bond1378 ↔ 1393 By similarity
Disulfide bond1395 ↔ 1406 By similarity
Disulfide bond1412 ↔ 1425 By similarity
Disulfide bond1419 ↔ 1434 By similarity
Disulfide bond1436 ↔ 1447 By similarity
Disulfide bond1453 ↔ 1465 By similarity
Disulfide bond1460 ↔ 1474 By similarity
Disulfide bond1476 ↔ 1489 By similarity
Disulfide bond1495 ↔ 1506 By similarity
Disulfide bond1501 ↔ 1515 By similarity
Disulfide bond1517 ↔ 1530 By similarity
Disulfide bond1536 ↔ 1547 By similarity
Disulfide bond1542 ↔ 1556 By similarity
Disulfide bond1558 ↔ 1571 By similarity
Disulfide bond1654 ↔ 1666 By similarity
Disulfide bond1661 ↔ 1675 By similarity
Disulfide bond1677 ↔ 1690 By similarity
Disulfide bond1696 ↔ 1708 By similarity
Disulfide bond1703 ↔ 1717 By similarity
Disulfide bond1719 ↔ 1732 By similarity
Disulfide bond1812 ↔ 1824 By similarity
Disulfide bond1819 ↔ 1833 By similarity
Disulfide bond1835 ↔ 1848 By similarity
Disulfide bond1854 ↔ 1867 By similarity
Disulfide bond1861 ↔ 1876 By similarity
Disulfide bond1878 ↔ 1890 By similarity
Disulfide bond1896 ↔ 1908 By similarity
Disulfide bond1903 ↔ 1917 By similarity
Disulfide bond1919 ↔ 1932 By similarity
Disulfide bond1938 ↔ 1948 By similarity
Disulfide bond1943 ↔ 1957 By similarity
Disulfide bond1959 ↔ 1971 By similarity
Disulfide bond1977 ↔ 1990 By similarity
Disulfide bond1985 ↔ 1999 By similarity
Disulfide bond2001 ↔ 2014 By similarity
Disulfide bond2020 ↔ 2032 By similarity
Disulfide bond2027 ↔ 2041 By similarity
Disulfide bond2043 ↔ 2054 By similarity
Disulfide bond2060 ↔ 2072 By similarity
Disulfide bond2067 ↔ 2081 By similarity
Disulfide bond2083 ↔ 2096 By similarity
Disulfide bond2175 ↔ 2187 By similarity
Disulfide bond2182 ↔ 2196 By similarity
Disulfide bond2198 ↔ 2211 By similarity
Disulfide bond2217 ↔ 2228 By similarity
Disulfide bond2223 ↔ 2237 By similarity
Disulfide bond2239 ↔ 2251 By similarity
Disulfide bond2257 ↔ 2268 By similarity
Disulfide bond2264 ↔ 2277 By similarity
Disulfide bond2279 ↔ 2292 By similarity
Disulfide bond2298 ↔ 2312 By similarity
Disulfide bond2305 ↔ 2321 By similarity
Disulfide bond2323 ↔ 2336 By similarity
Disulfide bond2342 ↔ 2354 By similarity
Disulfide bond2349 ↔ 2363 By similarity
Disulfide bond2365 ↔ 2378 By similarity
Disulfide bond2453 ↔ 2465 By similarity
Disulfide bond2460 ↔ 2474 By similarity
Disulfide bond2476 ↔ 2489 By similarity
Disulfide bond2495 ↔ 2506 By similarity
Disulfide bond2502 ↔ 2515 By similarity
Disulfide bond2517 ↔ 2530 By similarity
Disulfide bond2536 ↔ 2547 By similarity
Disulfide bond2543 ↔ 2556 By similarity
Disulfide bond2558 ↔ 2569 By similarity
Disulfide bond2575 ↔ 2588 By similarity
Disulfide bond2582 ↔ 2597 By similarity
Disulfide bond2599 ↔ 2612 By similarity
Disulfide bond2618 ↔ 2628 By similarity
Disulfide bond2624 ↔ 2637 By similarity
Disulfide bond2639 ↔ 2652 By similarity
Disulfide bond2658 ↔ 2669 By similarity
Disulfide bond2664 ↔ 2678 By similarity
Disulfide bond2680 ↔ 2693 By similarity
Disulfide bond2699 ↔ 2710 By similarity
Disulfide bond2706 ↔ 2719 By similarity
Disulfide bond2721 ↔ 2733 By similarity

Natural variations

Alternative sequence113 – 14533Missing in isoform 2.
VSP_037369
Alternative sequence1491 – 150616DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2.
VSP_037370
Alternative sequence1507 – 29121406Missing in isoform 2.
VSP_037371
Natural variant3911E → K in DA9.
VAR_015851
Natural variant5941T → S. Ref.1 Ref.8
VAR_054979
Natural variant6811R → H. Ref.8
VAR_054980
Natural variant7541G → S in DA9. Ref.12
VAR_058364
Natural variant9651V → I. Ref.7 Ref.8 Ref.11
Corresponds to variant rs154001 [ dbSNP | Ensembl ].
VAR_002349
Natural variant10571G → D in DA9. Ref.8 Ref.11
VAR_054981
Natural variant10911N → S in DA9. Ref.12
VAR_058365
Natural variant10931I → T in DA9. Ref.8 Ref.11
VAR_054982
Natural variant11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. Ref.9 Ref.12
VAR_010739
Natural variant11221S → P in DA9. Ref.12
VAR_058366
Natural variant11421C → F in DA9. Ref.10 Ref.11
VAR_010740
Natural variant11421C → R in DA9. Ref.12
VAR_058367
Natural variant11461Y → C in DA9. Ref.12
VAR_058368
Natural variant11561C → F in DA9. Ref.12
VAR_058369
Natural variant11611E → K in DA9. Ref.12
VAR_058370
Natural variant11791G → C in DA9. Ref.11
VAR_054983
Natural variant11981C → Y in DA9. Ref.11
VAR_054984
Natural variant12401C → R in DA9. Ref.11
VAR_054985
Natural variant12461C → F in DA9. Ref.12
VAR_058371
Natural variant12531C → W in DA9. Ref.10 Ref.11
Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
VAR_010741
Natural variant12531C → Y in DA9. Ref.7 Ref.11
VAR_002350
Natural variant12571C → W in DA9. Ref.11
VAR_054986
Natural variant12681C → R in DA9. Ref.11
VAR_054987
Natural variant13841C → F in DA9. Ref.12
VAR_058372
Natural variant13841C → Y in DA9. Ref.12
VAR_058373
Natural variant14081D → N in DA9. Ref.12
VAR_058374
Natural variant14251C → R in DA9. Ref.12
VAR_058375
Natural variant14341C → S in DA9. Ref.7 Ref.11
VAR_002351
Natural variant17721W → G. Ref.1 Ref.8
VAR_054988
Natural variant20621E → V Found in a renal cell carcinoma case; somatic mutation. Ref.13
VAR_064705
Natural variant22661F → L. Ref.1 Ref.8
VAR_054989
Natural variant22781T → M.
Corresponds to variant rs2307109 [ dbSNP | Ensembl ].
VAR_055415
Natural variant23111M → V.
Corresponds to variant rs32209 [ dbSNP | Ensembl ].
VAR_055416
Natural variant24281P → T. Ref.8
Corresponds to variant rs1801169 [ dbSNP | Ensembl ].
VAR_016143
Natural variant25801S → L. Ref.1
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_055417
Natural variant25811L → S.
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_054990
Natural variant27711S → P. Ref.1 Ref.8
Corresponds to variant rs1801170 [ dbSNP | Ensembl ].
VAR_014664

Experimental info

Sequence conflict1461I → L in BAG62163. Ref.2
Sequence conflict192 – 1954GPNR → AQP in AAA18950. Ref.1
Sequence conflict2431I → T in AAA18950. Ref.1
Sequence conflict2431I → T in BAG62163. Ref.2
Sequence conflict11611E → G in AAA18950. Ref.1
Sequence conflict11611E → G in CAB56757. Ref.4
Sequence conflict12441D → G in BAG62163. Ref.2
Sequence conflict14091L → R in CAB56757. Ref.4
Sequence conflict15031F → S in AAA18950. Ref.1
Sequence conflict25841A → G in AAA18950. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 26, 2009. Version 3.
Checksum: 0F0D78319E9911E6

FASTA2,912314,775
        10         20         30         40         50         60 
MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA TAGSEGGFLA 

        70         80         90        100        110        120 
PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG 

       130        140        150        160        170        180 
DGFCSRPNMC TCSSGQISST CGSKSIQQCS VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC 

       190        200        210        220        230        240 
ENGCQNGGRC IGPNRCACVY GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC 

       250        260        270        280        290        300 
ATIGRAWGHP CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE 

       310        320        330        340        350        360 
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV TSTDGSRCID 

       370        380        390        400        410        420 
QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT IPEACPVRGS EEYRRLCMDG 

       430        440        450        460        470        480 
LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG 

       490        500        510        520        530        540 
QGPIITGLTI LNQTIDICKH HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT 

       550        560        570        580        590        600 
SNPCTNGDCV NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC 

       610        620        630        640        650        660 
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA PNGRYCTDVD 

       670        680        690        700        710        720 
ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT HMRSTCYGGI KKGVCVRPFP 

       730        740        750        760        770        780 
GAVTKSECCC ANPDYGFGEP CQPCPAKNSA EFHGLCSSGV GITVDGRDIN ECALDPDICA 

       790        800        810        820        830        840 
NGICENLRGS YRCNCNSGYE PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG 

       850        860        870        880        890        900 
YVFRTETETC EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL 

       910        920        930        940        950        960 
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG VTCEDVNECE 

       970        980        990       1000       1010       1020 
VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM EQCYLKWDED ECIHPVPGKF 

      1030       1040       1050       1060       1070       1080 
RMDACCCAVG AAWGTECEEC PKPGTKEYET LCPRGAGFAN RGDVLTGRPF YKDINECKAF 

      1090       1100       1110       1120       1130       1140 
PGMCTYGKCR NTIGSFKCRC NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC 

      1150       1160       1170       1180       1190       1200 
ECFEGYESGF MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD 

      1210       1220       1230       1240       1250       1260 
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN GGCDTQCTNS 

      1270       1280       1290       1300       1310       1320 
EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT NIPGEYRCLC YDGFMASMDM 

      1330       1340       1350       1360       1370       1380 
KTCIDVNECD LNSNICMFGE CENTKGSFIC HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM 

      1390       1400       1410       1420       1430       1440 
HASCLNIPGS FKCSCREGWI GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF 

      1450       1460       1470       1480       1490       1500 
TGDGFTCSDV DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI 

      1510       1520       1530       1540       1550       1560 
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT PGRYECNCPP 

      1570       1580       1590       1600       1610       1620 
DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG VSRSSCCCSL GKAWGNPCET 

      1630       1640       1650       1660       1670       1680 
CPPVNSTEYY TLCPGGEGFR PNPITIILED IDECQELPGL CQGGNCINTF GSFQCECPQG 

      1690       1700       1710       1720       1730       1740 
YYLSEDTRIC EDIDECFAHP GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC 

      1750       1760       1770       1780       1790       1800 
YRSYNGTTCE NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD 

      1810       1820       1830       1840       1850       1860 
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED IDECSNGDNL 

      1870       1880       1890       1900       1910       1920 
CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP NVCSHGLCVD LQGSYQCICH 

      1930       1940       1950       1960       1970       1980 
NGFKASQDQT MCMDVDECER HPCGNGTCKN TVGSYNCLCY PGFELTHNND CLDIDECSSF 

      1990       2000       2010       2020       2030       2040 
FGQVCRNGRC FNEIGSFKCL CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR 

      2050       2060       2070       2080       2090       2100 
CICPPGYEVK SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR 

      2110       2120       2130       2140       2150       2160 
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA FQDLCPYGHG 

      2170       2180       2190       2200       2210       2220 
TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM GYNLDYTGVR CVDTDECSIG 

      2230       2240       2250       2260       2270       2280 
NPCGNGTCTN VIGSFECNCN EGFEPGPMMN CEDINECAQN PLLCAFRCMN TFGSYECTCP 

      2290       2300       2310       2320       2330       2340 
IGYALREDQK MCKDLDECAE GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN 

      2350       2360       2370       2380       2390       2400 
ECRTKPGICE NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS 

      2410       2420       2430       2440       2450       2460 
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI DECKVMPNLC 

      2470       2480       2490       2500       2510       2520 
TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK PCNYICKNTE GSYQCSCPRG 

      2530       2540       2550       2560       2570       2580 
YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT LGGFTCKCPP GFTQHHTACI DNNECGSQPS 

      2590       2600       2610       2620       2630       2640 
LCGAKGICQN TPGSFSCECQ RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP 

      2650       2660       2670       2680       2690       2700 
QGYIQHYQWN QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS 

      2710       2720       2730       2740       2750       2760 
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE VDEENALSPE 

      2770       2780       2790       2800       2810       2820 
ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD SPVNMKFNLS HLGSKEHILE 

      2830       2840       2850       2860       2870       2880 
LRPAIQPLNN HIRYVISQGN DDSVFRIHQR NGLSYLHTAK KKLMPGTYTL EITSIPLYKK 

      2890       2900       2910 
KELKKLEESN EDDYLLGELG EALRMRLQIQ LY 

« Hide

Isoform 2 [UniParc].

Checksum: 2B6620CFCA6F7A72
Show »

FASTA1,473157,690

References

« Hide 'large scale' references
[1]"Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices."
Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F.
J. Cell Biol. 124:855-863(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes."
Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W.
Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1).
Tissue: Aortic endothelium.
[6]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112.
Tissue: Liver.
[7]"Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly."
Putnam E.A., Zhang H., Ramirez F., Milewicz D.M.
Nat. Genet. 11:456-458(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DA9 TYR-1253 AND SER-1434, VARIANT ILE-965.
[8]"Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development."
Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M.
Am. J. Med. Genet. 78:350-355(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DA9 ASP-1057 AND THR-1093, VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
[9]"A single mutation that results in an Asp-to-His substitution and partial exon skipping in a family with congenital contractural arachnodactyly."
Babcock D., Gasner C., Francke U., Maslen C.
Hum. Genet. 103:22-28(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DA9 HIS-1115.
[10]"Two novel fibrillin-2 mutations in congenital contractural arachnodactyly."
Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M.
Am. J. Med. Genet. 92:7-12(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DA9 PHE-1142 AND TRP-1253.
[11]"Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype."
Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A., Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K., Ades L.C., Milewicz D.M.
Hum. Mutat. 19:39-48(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DA9 ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, VARIANT ILE-965.
[12]"Comprehensive clinical and molecular assessment of 32 probands with congenital contractural arachnodactyly: report of 14 novel mutations and review of the literature."
Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M., Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H., Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C., Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M.
Hum. Mutat. 30:334-341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DA9 SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146; PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
[13]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-2062.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03272 mRNA. Translation: AAA18950.1.
AK300440 mRNA. Translation: BAG62163.1.
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1.
AB209735 mRNA. Translation: BAD92972.1.
PIRA54105.
RefSeqNP_001990.2. NM_001999.3.
UniGeneHs.519294.

3D structure databases

ProteinModelPortalP35556.
SMRP35556. Positions 75-996, 1073-2335, 2338-2721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108495. 8 interactions.
IntActP35556. 3 interactions.
STRING9606.ENSP00000262464.

PTM databases

PhosphoSiteP35556.

Polymorphism databases

DMDM238054385.

Proteomic databases

PaxDbP35556.
PRIDEP35556.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
GeneID2201.
KEGGhsa:2201.
UCSCuc003kuu.3. human. [P35556-1]

Organism-specific databases

CTD2201.
GeneCardsGC05M127621.
H-InvDBHIX0005141.
HIX0137461.
HGNCHGNC:3604. FBN2.
HPACAB026401.
HPA012853.
MIM121050. phenotype.
612570. gene.
neXtProtNX_P35556.
Orphanet115. Congenital contractural arachnodactyly.
PharmGKBPA28017.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231768.
HOVERGENHBG005643.
InParanoidP35556.
OMASGRNCID.
OrthoDBEOG7RV9F6.
PhylomeDBP35556.
TreeFamTF316849.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP35556.
BgeeP35556.
CleanExHS_FBN2.
GenevestigatorP35556.

Family and domain databases

Gene3D3.90.290.10. 9 hits.
InterProIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PANTHERPTHR24039. PTHR24039. 1 hit.
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 41 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFPIRSF036312. Fibrillin. 1 hit.
SMARTSM00181. EGF. 3 hits.
SM00179. EGF_CA. 43 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2201.
NextBio8895.
PROP35556.
SOURCESearch...

Entry information

Entry nameFBN2_HUMAN
AccessionPrimary (citable) accession number: P35556
Secondary accession number(s): B4DU01, Q59ES6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM